The success of biomedical and biological research is highly dependent on determining the structures of proteins because essentially all properties of biological systems are expressed by proteins. However, the structures of many proteins cannot be determined with the commonly used methods. The overall goal of the research is to develop solid-state NMR spectroscopy as a method for determining the structures of proteins, extending the range of proteins that can be described at atomic resolution to include membrane proteins. This has been accomplished for selected examples, demonstrating the feasibility of preparation of oriented samples, spectroscopic experiments, and interpretive procedures. In order to make this method generally applicable for membrane proteins and other classes of proteins of interest to the biomedical research community, the most powerful instrumentation must be utilized in the development and application of the experimental procedures. There are three aspects to the research plan. The first is to upgrade substantially the instrumentation by replacing the magnet on an existing spectrometer with a high-field, wide-bore magnet; the second is to implement currently used experiments at the higher field and to develop new experiments that are feasible only at the higher field, especially those involving the measurement of (l)H spectral parameters, and the third is to participate in collaborative studies of membrane proteins that include the coat protein from filamentous bacteriophages and its precursor, procoat protein, magainin antibiotic peptides and their precursors, the nicotinic acetylcholine receptor, cytochrome b5, leader peptidase from E. coli, and gp4l from human immunodeficiency virus (HIV).